Oligomerization due to a-helix residues have been contributed to the toxin pore formation in insect larvae (Jimenez-Juarez et al.

In summary, substitution of the highly conserved H168 by Q or R in a-helix 5 of the Cry1Ac toxin resulted in changes in toxicity and stability which have helped to define better the role of this key amino acid residue in the properties and function of the Cry1Ac [delta]-endotoxin.

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